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The twin arginine protein transport (Tat) system transports folded proteins across cytoplasmic membranes of bacteria and thylakoid membranes of plants, and in Escherichia coli it comprises TatA, TatB and TatC components. In this study we show that the membrane extrinsic domain of TatB forms parallel contacts with at least one other TatB protein. Truncation of the C-terminal two thirds of TatB still allows complex formation with TatC, although protein transport is severely compromised. We were unable to isolate transport-inactive single codon substitution mutations in tatB suggesting that the precise amino acid sequence of TatB is not critical to its function.

Original publication

DOI

10.1016/j.febslet.2011.01.016

Type

Journal article

Journal

FEBS Lett

Publication Date

04/02/2011

Volume

585

Pages

478 - 484

Keywords

Codon, Escherichia coli, Escherichia coli Proteins, Genes, Reporter, Membrane Transport Proteins, Mutation, Protein Interaction Domains and Motifs, Protein Structure, Tertiary, Protein Subunits, Protein Transport, Recombinant Fusion Proteins, Secretory Pathway, Two-Hybrid System Techniques